Dipolar coupling-based electron paramagnetic resonance method for protease enzymatic characterization and inhibitor screening

Lu Yu, Aokun Liu, Bingbo Zhang, Jian Kuang, Xiaoqi Guo, Changlin Tian, Yi Lu

Research output: Contribution to journalArticlepeer-review

Abstract

Herein, we report an EPR-based method for protease enzymatic characterization and inhibitor screening. This method utilizes dual paramagnetically-labeled probes consisting of a nitroxide spin probe and a Gd3+ion flanking a peptide that could be specifically cleaved by protease caspase-3. Distance-dependent dipolar coupling between the two paramagnetic centers can be modulated by the protease cleavage activity, thus providing a straightforward and convenient method for protease activity detection using EPR spectroscopy under ambient conditions. Moreover, time-course monitoring of the protease-catalyzed cleavage reaction demonstrated that this EPR-based method could not only allow a direct quantitative enzymatic kinetic assessment, but also could be used for protease inhibitor screening, thus holding great potential in drug discovery studies.

Original languageEnglish (US)
Pages (from-to)9602-9605
Number of pages4
JournalChemical Communications
Volume57
Issue number75
DOIs
StatePublished - Sep 25 2021

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • General Chemistry
  • Ceramics and Composites
  • Metals and Alloys
  • Materials Chemistry
  • Surfaces, Coatings and Films
  • Catalysis

Fingerprint

Dive into the research topics of 'Dipolar coupling-based electron paramagnetic resonance method for protease enzymatic characterization and inhibitor screening'. Together they form a unique fingerprint.

Cite this